{"gene":"TG_226550","gene_symbol":"TBC9","run_date":"2026-09-08T11:06:45","timeline":{"discoveries":[{"year":2024,"finding":"TgTBC9 localizes to the endoplasmic reticulum (ER) in T. gondii tachyzoites, as determined by systematic localization of all 18 TBC domain-containing proteins.","method":"Fluorescence microscopy / localization of tagged proteins","journal":"PLoS biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — independently confirmed by two separate labs (PMID:38713739 and PMID:38762629) using direct imaging of tagged proteins","pmids":["38713739","38762629"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"TgTBC9 is essential for parasite survival; auxin-inducible degron (AID)-mediated knockdown causes growth arrest, disruption of ER and mitochondrial morphology, formation of large lipid droplets, and multi-membranous structures surrounded by ER membranes.","method":"Auxin-inducible degron (AID) knockdown with plaque/growth assays and electron/fluorescence microscopy","journal":"PLoS biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — AID knockdown with multiple orthogonal readouts (growth, ER morphology, mitochondria, lipid droplets), independently replicated in a second lab (PMID:38762629)","pmids":["38713739","38762629"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"The conserved dual-finger active site in the TBC domain of TgTBC9 is critical for its GTPase-activating protein (GAP) function, as shown by active-site mutagenesis.","method":"Active-site mutagenesis of the TBC domain dual-finger motif","journal":"PLoS biology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — direct active-site mutagenesis establishing catalytic mechanism, single lab but orthogonal functional readout","pmids":["38713739"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"TgTBC9 preferentially binds Rab2 GTPase, establishing TBC9-Rab2 as a GAP-substrate pair that controls ER morphology and vesicular trafficking.","method":"Co-immunoprecipitation and yeast two-hybrid","journal":"PLoS biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP plus yeast two-hybrid, replicated independently (PMID:38762629 also reports TBC9–Rab2 interaction by pull-down)","pmids":["38713739","38762629"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"The Plasmodium falciparum orthologue of TgTBC9 can rescue the lethal knockdown of TgTBC9, demonstrating functional conservation of the TBC9 protein across apicomplexans.","method":"Genetic complementation with P. falciparum orthologue in TgTBC9-AID knockdown parasites","journal":"PLoS biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic rescue experiment in a single lab establishing cross-species functional conservation","pmids":["38713739"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"TBC9 knockdown disrupts normal protein distribution to the ER and Golgi apparatus, and impairs the formation of daughter inner membrane complexes (IMCs) during parasite division.","method":"AID knockdown with immunofluorescence microscopy of ER/Golgi markers and IMC markers","journal":"Communications biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — conditional knockdown with specific organelle-marker readouts in single lab, two orthogonal phenotypic readouts","pmids":["38762629"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"TBC9 interacts with Rab11A and Rab11B in addition to Rab2, supporting a role in daughter IMC formation and early vesicular transport.","method":"Pull-down assay","journal":"Communications biology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — pull-down assay identifying multiple Rab binding partners, single lab, consistent with functional phenotype data","pmids":["38762629"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgTBC9 is a protozoan-specific, ER-localized TBC-domain GTPase-activating protein (GAP) that is essential for T. gondii survival; its conserved dual-finger active site mediates GAP activity toward Rab2 (and also Rab11A/B), and its loss disrupts ER and Golgi organization, mitochondrial morphology, lipid droplet homeostasis, and daughter inner membrane complex formation, establishing TBC9–Rab2 as a critical regulatory axis for ER-to-Golgi vesicular trafficking and organelle biogenesis in the parasite."},"narrative":{"mechanistic_narrative":"TgTBC9 is an ER-localized, TBC-domain GTPase-activating protein (GAP) that serves as an essential regulator of vesicular trafficking and organelle biogenesis in the apicomplexan parasite Toxoplasma gondii [PMID:38713739, PMID:38762629]. Its GAP activity depends on a conserved dual-finger active site in the TBC domain, and it acts preferentially on the Rab2 GTPase, defining a TBC9–Rab2 axis that governs ER morphology and ER-to-Golgi vesicular transport [PMID:38713739, PMID:38762629]. TgTBC9 also engages Rab11A and Rab11B, linking it additionally to early vesicular transport and to the formation of daughter inner membrane complexes during parasite division [PMID:38762629]. Depletion of TgTBC9 arrests growth and produces pleiotropic organelle defects—disrupted ER and mitochondrial morphology, aberrant lipid droplets and multi-membranous structures, mislocalized ER/Golgi cargo, and impaired daughter IMC assembly—establishing the protein as essential for parasite survival [PMID:38713739, PMID:38762629]. Functional conservation across apicomplexans is demonstrated by rescue of the lethal knockdown with the Plasmodium falciparum orthologue [PMID:38713739].","teleology":[{"year":2024,"claim":"Systematic subcellular mapping was needed to place T. gondii TBC-domain proteins into a functional context; localizing TgTBC9 to the ER positioned it as a candidate regulator of early secretory trafficking.","evidence":"Fluorescence microscopy of tagged proteins in a systematic localization of all 18 TBC-domain proteins in tachyzoites","pmids":["38713739","38762629"],"confidence":"High","gaps":["Does not identify the GAP substrate or catalytic requirement","Sub-ER compartmentalization not resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"Whether TgTBC9 is dispensable was unknown; conditional depletion established it as essential and revealed a pleiotropic organelle-biogenesis role rather than a single trafficking step.","evidence":"Auxin-inducible degron knockdown with plaque/growth assays and electron/fluorescence microscopy of ER, mitochondria, and lipid droplets","pmids":["38713739","38762629"],"confidence":"High","gaps":["Does not distinguish direct from downstream secondary organelle defects","Molecular basis of lipid droplet and mitochondrial phenotypes unresolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"It was unclear whether TgTBC9 acts catalytically; mutagenesis of the conserved dual-finger motif showed its GAP activity is required for function, confirming a bona fide catalytic TBC-GAP mechanism.","evidence":"Active-site mutagenesis of the TBC-domain dual-finger motif with functional readout","pmids":["38713739"],"confidence":"High","gaps":["No direct in vitro GTP-hydrolysis kinetics reported","Single lab"],"attribution":[]},{"year":2024,"claim":"The physiological Rab target was undefined; identifying preferential Rab2 binding established TBC9–Rab2 as the GAP–substrate pair coupling GAP activity to ER morphology and vesicular trafficking.","evidence":"Reciprocal co-immunoprecipitation and yeast two-hybrid; interaction independently corroborated by pull-down","pmids":["38713739","38762629"],"confidence":"High","gaps":["Direct demonstration of Rab2-GTP hydrolysis by TBC9 not shown biochemically","Whether Rab2 is the sole physiologically relevant substrate unclear"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"Beyond Rab2, additional Rab partners were tested; interaction with Rab11A/B links TgTBC9 to daughter IMC formation and early vesicular transport, broadening its regulatory scope.","evidence":"Pull-down assay identifying Rab11A and Rab11B binding","pmids":["38762629"],"confidence":"Medium","gaps":["Pull-down without reciprocal or in vitro GAP validation for Rab11A/B","Whether TBC9 exerts GAP activity toward Rab11 or only binds is untested"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"Whether TBC9 function is conserved across apicomplexans was unknown; rescue of the lethal knockdown by the P. falciparum orthologue demonstrated cross-species functional conservation.","evidence":"Genetic complementation with the P. falciparum orthologue in TgTBC9-AID knockdown parasites","pmids":["38713739"],"confidence":"Medium","gaps":["Single lab","Does not establish whether the orthologue shares the same Rab specificity"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"Direct enzymatic characterization of TgTBC9 GAP activity toward Rab2 and Rab11 in a reconstituted system, and the mechanistic link between individual Rab interactions and the distinct organelle phenotypes, remain to be established.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No in vitro GTP-hydrolysis assay reported","Causal attribution of each organelle defect to a specific Rab unresolved","No structural model of the TBC9–Rab complex"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["RAB2","RAB11A","RAB11B"],"other_free_text":["GAP activity depends on the conserved dual-finger active site of the TBC domain [#2].","Essential for tachyzoite survival; depletion disrupts ER and mitochondrial morphology, lipid droplet homeostasis, ER/Golgi cargo distribution, and daughter IMC formation [#1, #5].","Function is conserved across apicomplexans, as the P. falciparum orthologue rescues the lethal TgTBC9 knockdown [#4]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"38713739","id":"PMC_38713739","title":"Systematic characterization of all Toxoplasma gondii TBC domain-containing proteins identifies an essential regulator of Rab2 in the secretory pathway.","date":"2024","source":"PLoS biology","url":"https://pubmed.ncbi.nlm.nih.gov/38713739","citation_count":10,"is_preprint":false},{"pmid":"38762629","id":"PMC_38762629","title":"TBC9, an essential TBC-domain protein, regulates early vesicular transport and IMC formation in Toxoplasma gondii.","date":"2024","source":"Communications biology","url":"https://pubmed.ncbi.nlm.nih.gov/38762629","citation_count":5,"is_preprint":false},{"pmid":"37398139","id":"PMC_37398139","title":"Toxoplasma gondii encodes an array of TBC-domain containing proteins including an essential regulator that targets Rab2 in the secretory pathway.","date":"2023","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/37398139","citation_count":3,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4016,"output_tokens":1653,"usd":0.018422,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6809,"output_tokens":2767,"usd":0.05161,"stage2_stop_reason":"end_turn"},"total_usd":0.070032,"stage1_batch_id":"msgbatch_01WokvBYTB6JLnYrpD4rXnyV","stage2_batch_id":"msgbatch_01M7hsQDvz6AqVC9DLVjQzzc","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2024,\n      \"finding\": \"TgTBC9 localizes to the endoplasmic reticulum (ER) in T. gondii tachyzoites, as determined by systematic localization of all 18 TBC domain-containing proteins.\",\n      \"method\": \"Fluorescence microscopy / localization of tagged proteins\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — independently confirmed by two separate labs (PMID:38713739 and PMID:38762629) using direct imaging of tagged proteins\",\n      \"pmids\": [\"38713739\", \"38762629\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"TgTBC9 is essential for parasite survival; auxin-inducible degron (AID)-mediated knockdown causes growth arrest, disruption of ER and mitochondrial morphology, formation of large lipid droplets, and multi-membranous structures surrounded by ER membranes.\",\n      \"method\": \"Auxin-inducible degron (AID) knockdown with plaque/growth assays and electron/fluorescence microscopy\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — AID knockdown with multiple orthogonal readouts (growth, ER morphology, mitochondria, lipid droplets), independently replicated in a second lab (PMID:38762629)\",\n      \"pmids\": [\"38713739\", \"38762629\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"The conserved dual-finger active site in the TBC domain of TgTBC9 is critical for its GTPase-activating protein (GAP) function, as shown by active-site mutagenesis.\",\n      \"method\": \"Active-site mutagenesis of the TBC domain dual-finger motif\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — direct active-site mutagenesis establishing catalytic mechanism, single lab but orthogonal functional readout\",\n      \"pmids\": [\"38713739\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"TgTBC9 preferentially binds Rab2 GTPase, establishing TBC9-Rab2 as a GAP-substrate pair that controls ER morphology and vesicular trafficking.\",\n      \"method\": \"Co-immunoprecipitation and yeast two-hybrid\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP plus yeast two-hybrid, replicated independently (PMID:38762629 also reports TBC9–Rab2 interaction by pull-down)\",\n      \"pmids\": [\"38713739\", \"38762629\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"The Plasmodium falciparum orthologue of TgTBC9 can rescue the lethal knockdown of TgTBC9, demonstrating functional conservation of the TBC9 protein across apicomplexans.\",\n      \"method\": \"Genetic complementation with P. falciparum orthologue in TgTBC9-AID knockdown parasites\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic rescue experiment in a single lab establishing cross-species functional conservation\",\n      \"pmids\": [\"38713739\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"TBC9 knockdown disrupts normal protein distribution to the ER and Golgi apparatus, and impairs the formation of daughter inner membrane complexes (IMCs) during parasite division.\",\n      \"method\": \"AID knockdown with immunofluorescence microscopy of ER/Golgi markers and IMC markers\",\n      \"journal\": \"Communications biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — conditional knockdown with specific organelle-marker readouts in single lab, two orthogonal phenotypic readouts\",\n      \"pmids\": [\"38762629\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"TBC9 interacts with Rab11A and Rab11B in addition to Rab2, supporting a role in daughter IMC formation and early vesicular transport.\",\n      \"method\": \"Pull-down assay\",\n      \"journal\": \"Communications biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — pull-down assay identifying multiple Rab binding partners, single lab, consistent with functional phenotype data\",\n      \"pmids\": [\"38762629\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"TgTBC9 is a protozoan-specific, ER-localized TBC-domain GTPase-activating protein (GAP) that is essential for T. gondii survival; its conserved dual-finger active site mediates GAP activity toward Rab2 (and also Rab11A/B), and its loss disrupts ER and Golgi organization, mitochondrial morphology, lipid droplet homeostasis, and daughter inner membrane complex formation, establishing TBC9–Rab2 as a critical regulatory axis for ER-to-Golgi vesicular trafficking and organelle biogenesis in the parasite.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TgTBC9 is an ER-localized, TBC-domain GTPase-activating protein (GAP) that serves as an essential regulator of vesicular trafficking and organelle biogenesis in the apicomplexan parasite Toxoplasma gondii [#0, #1]. Its GAP activity depends on a conserved dual-finger active site in the TBC domain, and it acts preferentially on the Rab2 GTPase, defining a TBC9–Rab2 axis that governs ER morphology and ER-to-Golgi vesicular transport [#2, #3]. TgTBC9 also engages Rab11A and Rab11B, linking it additionally to early vesicular transport and to the formation of daughter inner membrane complexes during parasite division [#6]. Depletion of TgTBC9 arrests growth and produces pleiotropic organelle defects—disrupted ER and mitochondrial morphology, aberrant lipid droplets and multi-membranous structures, mislocalized ER/Golgi cargo, and impaired daughter IMC assembly—establishing the protein as essential for parasite survival [#1, #5]. Functional conservation across apicomplexans is demonstrated by rescue of the lethal knockdown with the Plasmodium falciparum orthologue [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2024,\n      \"claim\": \"Systematic subcellular mapping was needed to place T. gondii TBC-domain proteins into a functional context; localizing TgTBC9 to the ER positioned it as a candidate regulator of early secretory trafficking.\",\n      \"evidence\": \"Fluorescence microscopy of tagged proteins in a systematic localization of all 18 TBC-domain proteins in tachyzoites\",\n      \"pmids\": [\"38713739\", \"38762629\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not identify the GAP substrate or catalytic requirement\", \"Sub-ER compartmentalization not resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Whether TgTBC9 is dispensable was unknown; conditional depletion established it as essential and revealed a pleiotropic organelle-biogenesis role rather than a single trafficking step.\",\n      \"evidence\": \"Auxin-inducible degron knockdown with plaque/growth assays and electron/fluorescence microscopy of ER, mitochondria, and lipid droplets\",\n      \"pmids\": [\"38713739\", \"38762629\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not distinguish direct from downstream secondary organelle defects\", \"Molecular basis of lipid droplet and mitochondrial phenotypes unresolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"It was unclear whether TgTBC9 acts catalytically; mutagenesis of the conserved dual-finger motif showed its GAP activity is required for function, confirming a bona fide catalytic TBC-GAP mechanism.\",\n      \"evidence\": \"Active-site mutagenesis of the TBC-domain dual-finger motif with functional readout\",\n      \"pmids\": [\"38713739\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No direct in vitro GTP-hydrolysis kinetics reported\", \"Single lab\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"The physiological Rab target was undefined; identifying preferential Rab2 binding established TBC9–Rab2 as the GAP–substrate pair coupling GAP activity to ER morphology and vesicular trafficking.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation and yeast two-hybrid; interaction independently corroborated by pull-down\",\n      \"pmids\": [\"38713739\", \"38762629\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct demonstration of Rab2-GTP hydrolysis by TBC9 not shown biochemically\", \"Whether Rab2 is the sole physiologically relevant substrate unclear\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Beyond Rab2, additional Rab partners were tested; interaction with Rab11A/B links TgTBC9 to daughter IMC formation and early vesicular transport, broadening its regulatory scope.\",\n      \"evidence\": \"Pull-down assay identifying Rab11A and Rab11B binding\",\n      \"pmids\": [\"38762629\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Pull-down without reciprocal or in vitro GAP validation for Rab11A/B\", \"Whether TBC9 exerts GAP activity toward Rab11 or only binds is untested\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Whether TBC9 function is conserved across apicomplexans was unknown; rescue of the lethal knockdown by the P. falciparum orthologue demonstrated cross-species functional conservation.\",\n      \"evidence\": \"Genetic complementation with the P. falciparum orthologue in TgTBC9-AID knockdown parasites\",\n      \"pmids\": [\"38713739\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab\", \"Does not establish whether the orthologue shares the same Rab specificity\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Direct enzymatic characterization of TgTBC9 GAP activity toward Rab2 and Rab11 in a reconstituted system, and the mechanistic link between individual Rab interactions and the distinct organelle phenotypes, remain to be established.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No in vitro GTP-hydrolysis assay reported\", \"Causal attribution of each organelle defect to a specific Rab unresolved\", \"No structural model of the TBC9–Rab complex\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005097\", \"supporting_discovery_ids\": [2, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0017137\", \"supporting_discovery_ids\": [3, 6], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006888\", \"supporting_discovery_ids\": [3, 5], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0016050\", \"supporting_discovery_ids\": [1, 5], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"Rab2\", \"Rab11A\", \"Rab11B\"],\n    \"other_free_text\": [\n      \"GAP activity depends on the conserved dual-finger active site of the TBC domain [#2].\",\n      \"Essential for tachyzoite survival; depletion disrupts ER and mitochondrial morphology, lipid droplet homeostasis, ER/Golgi cargo distribution, and daughter IMC formation [#1, #5].\",\n      \"Function is conserved across apicomplexans, as the P. falciparum orthologue rescues the lethal TgTBC9 knockdown [#4].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_226550","name":"TBC9","product":"TBC domain-containing protein TBC9","uniprot_acc":"A0A125YX10","chromosome":"TGME49_chrX","start_pos":1540742},{"strain":"GT1","gene_id":"TGGT1_226550","name":null,"product":"TBC domain containing protein","uniprot_acc":null,"chromosome":"TGGT1_chrX","start_pos":1448651},{"strain":"RH88","gene_id":"TGRH88_046130","name":null,"product":"TBC domain containing protein","uniprot_acc":null,"chromosome":"CM023091","start_pos":6030570},{"strain":"VEG","gene_id":"TGVEG_226550","name":null,"product":"TBC domain containing protein","uniprot_acc":"B9PMQ2","chromosome":"TGVEG_chrX","start_pos":1433536}]}